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            <front>

                <journal-meta>
                                                                <journal-id>biotech studies</journal-id>
            <journal-title-group>
                                                                                    <journal-title>Biotech Studies</journal-title>
            </journal-title-group>
                            <issn pub-type="ppub">2687-3761</issn>
                                        <issn pub-type="epub">2757-5233</issn>
                                                                                            <publisher>
                    <publisher-name>Tarla Bitkileri Merkez Araştırma Enstitüsü</publisher-name>
                </publisher>
                    </journal-meta>
                <article-meta>
                                        <article-id pub-id-type="doi">10.38042/biotechstudies.1601273</article-id>
                                                                <article-categories>
                                            <subj-group  xml:lang="en">
                                                            <subject>Enzymes</subject>
                                                            <subject>Bioprocessing, Bioproduction and Bioproducts</subject>
                                                    </subj-group>
                                            <subj-group  xml:lang="tr">
                                                            <subject>Enzimler</subject>
                                                            <subject>Biyoişlem, Biyoüretim ve Biyoürünler</subject>
                                                    </subj-group>
                                    </article-categories>
                                                                                                                                                        <title-group>
                                                                                                                                                            <article-title>Bench scale production of butyrohydroxamic acid using amidotransferase activity of amidase from whole resting cell Bacillus sp. APB-6.</article-title>
                                                                                                    </title-group>
            
                                                    <contrib-group content-type="authors">
                                                                        <contrib contrib-type="author">
                                                                    <contrib-id contrib-id-type="orcid">
                                        https://orcid.org/0000-0001-9960-6122</contrib-id>
                                                                <name>
                                    <surname>Kumari</surname>
                                    <given-names>Pankaj</given-names>
                                </name>
                                                                    <aff>1Department of Biotechnology, Multi Faculty Building</aff>
                                                            </contrib>
                                                    <contrib contrib-type="author">
                                                                    <contrib-id contrib-id-type="orcid">
                                        https://orcid.org/0000-0003-2823-0062</contrib-id>
                                                                <name>
                                    <surname>Pal</surname>
                                    <given-names>Mohinder</given-names>
                                </name>
                                                                    <aff>Department of Biotechnology, Chandigarh College of Technology, Chandigarh Group of Colleges</aff>
                                                            </contrib>
                                                    <contrib contrib-type="author">
                                                                    <contrib-id contrib-id-type="orcid">
                                        https://orcid.org/0000-0002-9432-2523</contrib-id>
                                                                <name>
                                    <surname>Thakur</surname>
                                    <given-names>Abhishek</given-names>
                                </name>
                                                                    <aff>Department of Biotechnology, Multi Faculty Building (Phase-I), Gyan Path, HP University Campus</aff>
                                                            </contrib>
                                                    <contrib contrib-type="author">
                                                                <name>
                                    <surname>Chand</surname>
                                    <given-names>Duni</given-names>
                                </name>
                                                                    <aff>Department of Biotechnology, Multi Faculty Building (Phase-I), Gyan Path, HP University Campus</aff>
                                                            </contrib>
                                                                                </contrib-group>
                        
                                        <pub-date pub-type="pub" iso-8601-date="20241231">
                    <day>12</day>
                    <month>31</month>
                    <year>2024</year>
                </pub-date>
                                        <volume>33</volume>
                                        <issue>2</issue>
                                        <fpage>112</fpage>
                                        <lpage>118</lpage>
                        
                        <history>
                                    <date date-type="received" iso-8601-date="20240119">
                        <day>01</day>
                        <month>19</month>
                        <year>2024</year>
                    </date>
                                                    <date date-type="accepted" iso-8601-date="20241104">
                        <day>11</day>
                        <month>04</month>
                        <year>2024</year>
                    </date>
                            </history>
                                        <permissions>
                    <copyright-statement>Copyright © 1992, Biotech Studies</copyright-statement>
                    <copyright-year>1992</copyright-year>
                    <copyright-holder>Biotech Studies</copyright-holder>
                </permissions>
            
                                                                                                                        <abstract><p>Butyrohydroxamic acid is a hydroxamic acid that has various biological and pharmacological applications. This study reports the bioconversion of butyramide and hydroxylamine to butyrohydroxamic acid with the help of amidase of Bacillus sp. APB-6, which has amidotransferase activity. Optimal conditions for the reaction were determined as 100/1200 mM butyramide/hydroxylamine ratio, incubation time 5 hr, pH 9.5, temperature 55°C, and resting cell concentration of 1.578 mg dcw ml-1. Under these conditions, the complete conversion of butyramide to butyrohydroxamic acid was attained in a 50 ml flask scale. The batch reaction was preferred over fed-batch reaction for scaling up the process to a 1 L scale, and the reaction time was reduced by 30 minutes. The final product yield was 10.23 g butyrohydroxamic acid with 95% purity, volumetric productivity of 2.273 g/L/h and 1.44 g/g/h catalytic productivity. The amidase used in this study showed high amidotransferase activity along with the industrially relevant process for the production of butyrohydroxamic acid. The NMR spectrum of the recovered product confirmed its identity as butyrohydroxamic acid.</p></abstract>
                                                            
            
                                                                                        <kwd-group>
                                                    <kwd>Butyrohydroxamic acid</kwd>
                                                    <kwd>  Amidotransferase activity</kwd>
                                                    <kwd>  Fed-batch</kwd>
                                                    <kwd>  Whole resting cell</kwd>
                                                    <kwd>  NMR</kwd>
                                            </kwd-group>
                            
                                                                                                                                                    </article-meta>
    </front>
    <back>
                            <ref-list>
                                    <ref id="ref1">
                        <label>1</label>
                        <mixed-citation publication-type="journal">Adebayo, G. P., Oduselu, G. O., Aderohunmu, D. V., Klika, K. D., Olasehinde, G. I., Ajani, O. O., &amp; Adebiyi, E. (2024). Structure-based design, and development of amidinyl, amidoximyl and hydroxamic acid based organic molecules as novel antimalarial drug candidates. Arabian Journal of Chemistry, 17(2), 105573. https://doi.org/10.1016/j.arabjc.2023.105573</mixed-citation>
                    </ref>
                                    <ref id="ref2">
                        <label>2</label>
                        <mixed-citation publication-type="journal">Agarwal, S., Gupta, M., &amp; Choudhury, B. (2013). Bioprocess development for nicotinic acid hydroxamate synthesis by acyltransferase activity of Bacillus smithii strain IITR6b2. Journal of Industrial Microbiology and Biotechnology,40(9),937-946. https://doi.org/10.1007/s10295-013-1299-x</mixed-citation>
                    </ref>
                                    <ref id="ref3">
                        <label>3</label>
                        <mixed-citation publication-type="journal">Bhatia, R. K., Bhatia, S. K., Kumar, V., &amp; Bhalla, T. C. (2015). Bi-substrate kinetic analysis of acyl transfer activity of purified amidase from Pseudomonas putida BR-1. Catalysis Letters, 145, 1033-1040. https://doi.org/10.1007/s10562-014-1467-2</mixed-citation>
                    </ref>
                                    <ref id="ref4">
                        <label>4</label>
                        <mixed-citation publication-type="journal">Bhatia, R. K., Bhatia, S. K., Mehta, P. K., &amp; Bhalla, T. C. (2013). Bench scale production of benzohydroxamic acid using acyl transfer activity of amidase from Alcaligenes sp. MTCC 10674. Journal of Industrial Microbiology and Biotechnology, 40(1), 21-27.
https://doi.org/10.1007/s10295-012-1206-x</mixed-citation>
                    </ref>
                                    <ref id="ref5">
                        <label>5</label>
                        <mixed-citation publication-type="journal">Boodhoo, K. V. K., Flickinger, M. C., Woodley, J. M., &amp; Emanuelsson, E. A. C. (2022). Bioprocess intensification: A route to efficient and sustainable biocatalytic transformations for the future. Chemical Engineering and Processing-Process Intensification, 172, 108793. 
https://doi.org/10.1016/j.cep.2022.108793</mixed-citation>
                    </ref>
                                    <ref id="ref6">
                        <label>6</label>
                        <mixed-citation publication-type="journal">Brammar, W. J., &amp; Clarke, P. H. (1964). Induction and repression of Pseudomonas aeruginosa amidase. Microbiology,37(3),307-319. https://doi.org/10.1099/00221287-37-3-307</mixed-citation>
                    </ref>
                                    <ref id="ref7">
                        <label>7</label>
                        <mixed-citation publication-type="journal">Devi, N., Patel, S. K., Kumar, P., Singh, A., Thakur, N., Lata, J., Pandey, D., Thakur, V., &amp; Chand, D. (2022). Bioprocess scale-up for acetohydroxamic acid production by hyperactive acyltransferase of immobilized Rhodococcus pyridinivorans. Catalysis Letters, 152(4), 944-953. https://doi.org/10.1007/s10562-021-03696-4</mixed-citation>
                    </ref>
                                    <ref id="ref8">
                        <label>8</label>
                        <mixed-citation publication-type="journal">Fournand, D., Bigey, F., Ratomahenina, R., Arnaud, A., &amp; Galzy, P. (1997). Biocatalyst improvement for the production of short-chain hydroxamic acids. Enzyme and Microbial Technology, 20(6), 424-431. https://doi.org/10.1016/S0141-0229(96)00170-6</mixed-citation>
                    </ref>
                                    <ref id="ref9">
                        <label>9</label>
                        <mixed-citation publication-type="journal">Kanwar, K., Sharma, D., Singh, H., Pal, M., Bandhu, R., &amp; Azmi, W. (2024). In vitro effects of alginate lyase SG4+ produced by Paenibacillus lautus alone and combined with antibiotics on biofilm formation by mucoid Pseudomonas aeruginosa. Brazilian Journal of Microbiology, 1-15. https://doi.org/10.1007/s42770-024-01334-w</mixed-citation>
                    </ref>
                                    <ref id="ref10">
                        <label>10</label>
                        <mixed-citation publication-type="journal">Končić, M. Z., Barbarić, M., Perković, I., &amp; Zorc, B. (2011). Antiradical, chelating and antioxidant activities of hydroxamic acids and hydroxyureas. Molecules, 16(8),6232-6242. https://doi.org/10.3390/molecules16086232</mixed-citation>
                    </ref>
                                    <ref id="ref11">
                        <label>11</label>
                        <mixed-citation publication-type="journal">Kumari, P., Chand, D. (2017) Immobilization of whole resting cell of Bacillus sp. APB-6 exhibiting amidotransferase activity on sodium alginate beads and its comparative study with whole resting cells. Journal of Innovations in Pharmaceutical and Biological Sciences, 4:121-127. https://jipbs.com/index.php/journal/article/view/247</mixed-citation>
                    </ref>
                                    <ref id="ref12">
                        <label>12</label>
                        <mixed-citation publication-type="journal">Kumari. P., Devi, N., &amp; Chand, D. (2017) Enhanced production of amidotransferase from Bacillus sp. ABP-6 by optimization of nutritional parameters using statistical experimental design. International Journal of Engineering Science Invention, 12-22. https://www.ijesi.org/papers/Vol(6)9/Version4/B0609041222.pdf</mixed-citation>
                    </ref>
                                    <ref id="ref13">
                        <label>13</label>
                        <mixed-citation publication-type="journal">Lin, H., Xu, P., &amp; Huang, M. (2022). Structure-based molecular insights into matrix metalloproteinase inhibitors in cancer treatments. Future Medicinal Chemistry, 14(1), 35-51. https://doi.org/10.4155/fmc-2021-0246</mixed-citation>
                    </ref>
                                    <ref id="ref14">
                        <label>14</label>
                        <mixed-citation publication-type="journal">Mountanea, O. G., Mantzourani, C., Kokotou, M. G., Kokotos, C. G., &amp; Kokotos, G. (2023). Sunlight‐or UVA‐Light‐Mediated Synthesis of Hydroxamic Acids from Carboxylic Acids. European Journal of Organic Chemistry,26(13),e202300046. https://doi.org/10.1002/ejoc.202300046</mixed-citation>
                    </ref>
                                    <ref id="ref15">
                        <label>15</label>
                        <mixed-citation publication-type="journal">Pandey, D., Singh, R., &amp; Chand, D. (2011). An improved bioprocess for synthesis of acetohydroxamic acid using DTT (dithiothreitol) treated resting cells of Bacillus sp. APB-6. Bioresource Technology, 102(11), 6579-6586. https://doi.org/10.1016/j.biortech.2011.03.071</mixed-citation>
                    </ref>
                                    <ref id="ref16">
                        <label>16</label>
                        <mixed-citation publication-type="journal">Sharma, H., Singh, R. V., Ganjoo, A., Kumar, A., Singh, R., &amp; Babu, V. (2022). Development of effective biotransformation process for benzohydroxamic acid production using Bacillus smithii IIIMB2907. 3 Biotech, 12(2), 44. https://doi.org/10.1007/s13205-022-03109-2</mixed-citation>
                    </ref>
                                    <ref id="ref17">
                        <label>17</label>
                        <mixed-citation publication-type="journal">Sharma, M., Sharma, N. N., &amp; Bhalla, T. C. (2012). Biotransformation of acetamide to acetohydroxamic acid at bench scale using acyl transferase activity of amidase of Geobacillus pallidus BTP-5x MTCC 9225. Indian Journal of Microbiology, 52, 76-82. 
https://doi.org/10.1007/s12088-011-0211-5</mixed-citation>
                    </ref>
                                    <ref id="ref18">
                        <label>18</label>
                        <mixed-citation publication-type="journal">Singh, R. V., Sharma, H., Ganjoo, A., Kumar, A., &amp; Babu, V. (2020). Novel amidase catalysed process for the synthesis of vorinostat drug. Journal of Applied Microbiology,129(6),1589-1597. https://doi.org/10.1111/jam.14753</mixed-citation>
                    </ref>
                                    <ref id="ref19">
                        <label>19</label>
                        <mixed-citation publication-type="journal">Syed, Z., Sonu, K., Dongre, A., Sharma, G., &amp; Sogani, M. (2020). A review on hydroxamic acids: Widespectrum chemotherapeutic agents. International Journal of Biology and Biomedical Engineering, 14, 75-88. https://doi.org/10.46300/91011.2020.14.12</mixed-citation>
                    </ref>
                                    <ref id="ref20">
                        <label>20</label>
                        <mixed-citation publication-type="journal">Victorino da Silva Amatto, I., Gonsales da Rosa‐Garzon, N., Antonio de Oliveira Simoes, F., Santiago, F., Pereira da Silva Leite, N., Raspante Martins, J., &amp; Cabral, H. (2022). Enzyme engineering and its industrial applications. Biotechnology and Applied Biochemistry, 69(2), 389-409. https://doi.org/10.1002/bab.2117</mixed-citation>
                    </ref>
                                    <ref id="ref21">
                        <label>21</label>
                        <mixed-citation publication-type="journal">Wang, M., Tang, T., Huang, Z., Li, R., Ling, D., Zhu, J., ... &amp; Li, X. (2022). Design and synthesis of novel hydroxamic acid derivatives based on quisinostat as promising antimalarial agents with improved safety. Acta Materia Medica, 1(2), 212-223. https://doi.org/10.15212/AMM-2022-0007</mixed-citation>
                    </ref>
                                    <ref id="ref22">
                        <label>22</label>
                        <mixed-citation publication-type="journal">Wu, Z., Liu, C., Zhang, Z., Zheng, R., &amp; Zheng, Y. (2020). Amidase as a versatile tool in amide-bond cleavage: From molecular features to biotechnological applications. Biotechnology Advances, 43, 107574. https://doi.org/10.1016/j.biotechadv.2020.107574</mixed-citation>
                    </ref>
                                    <ref id="ref23">
                        <label>23</label>
                        <mixed-citation publication-type="journal">Xi, L., Tan, W., Li, J., Qu, J., &amp; Liu, J. (2021). Cloning and characterization of a novel thermostable amidase, Xam, from Xinfangfangia sp. DLY26. Biotechnology Letters,43, 1395-1402. https://doi.org/10.1007/s10529-021-03124-y</mixed-citation>
                    </ref>
                            </ref-list>
                    </back>
    </article>
